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Q9Y657

- SPIN1_HUMAN

UniProt

Q9Y657 - SPIN1_HUMAN

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Protein
Spindlin-1
Gene
SPIN1, OCR, SPIN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (1 Publication). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (1 Publication). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei173 – 1731Histone H3K4me3 and H3R8me2a
Binding sitei180 – 1801Histone H3K4me3 and H3R8me2a
Binding sitei184 – 1841Histone H3K4me3 and H3R8me2a

GO - Molecular functioni

  1. methylated histone binding Source: UniProtKB
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. chromatin modification Source: UniProtKB-KW
  3. gamete generation Source: InterPro
  4. meiotic nuclear division Source: UniProtKB-KW
  5. multicellular organismal development Source: UniProtKB-KW
  6. positive regulation of Wnt signaling pathway Source: UniProtKB
  7. rRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein

Keywords - Biological processi

Cell cycle, Meiosis, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Spindlin-1
Alternative name(s):
Ovarian cancer-related protein
Spindlin1
Gene namesi
Name:SPIN1
Synonyms:OCR, SPIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11243. SPIN1.

Subcellular locationi

Nucleus. Nucleusnucleolus 2 Publications

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
  2. nucleus Source: LIFEdb
  3. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721W → A or R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication
Mutagenesisi98 – 981Y → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication
Mutagenesisi109 – 1091S → A: Impaired phosphorylation. 1 Publication
Mutagenesisi124 – 1241S → A: Impaired phosphorylation. 1 Publication
Mutagenesisi141 – 1411F → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications
Mutagenesisi142 – 1421E → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication
Mutagenesisi170 – 1701Y → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications
Mutagenesisi177 – 1771Y → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication
Mutagenesisi184 – 1841D → A or R: Impaired binding to histone H3K4me3 and H3R8me2a. 2 Publications
Mutagenesisi189 – 1891D → A or R: Impaired binding to histone H3K4me3. 1 Publication
Mutagenesisi251 – 2511F → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication

Organism-specific databases

PharmGKBiPA162404504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Spindlin-1
PRO_0000181367Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysine By similarity
Modified residuei109 – 1091Phosphoserine; by AURKA1 Publication
Modified residuei124 – 1241Phosphoserine; by AURKA3 Publications
Modified residuei199 – 1991Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated during oocyte meiotic maturation By similarity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y657.
PaxDbiQ9Y657.
PRIDEiQ9Y657.

PTM databases

PhosphoSiteiQ9Y657.

Expressioni

Tissue specificityi

Highly expressed in ovarian cancer tissues.1 Publication

Gene expression databases

BgeeiQ9Y657.
CleanExiHS_SPIN1.
GenevestigatoriQ9Y657.

Organism-specific databases

HPAiHPA000162.

Interactioni

Subunit structurei

Homodimer; may form higher-order oligomers (1 Publication). Interacts with TCF7L2/TCF4; the interaction is direct. Interacts with HABP4 and SERBP1.3 Publications

Protein-protein interaction databases

BioGridi116130. 15 interactions.
DIPiDIP-40062N.
IntActiQ9Y657. 6 interactions.
MINTiMINT-1428826.
STRINGi9606.ENSP00000365019.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 627
Beta strandi65 – 673
Beta strandi70 – 7910
Beta strandi87 – 915
Beta strandi98 – 1003
Turni102 – 1043
Beta strandi108 – 11710
Helixi126 – 1327
Beta strandi136 – 1427
Beta strandi144 – 1463
Beta strandi148 – 15811
Beta strandi160 – 1623
Beta strandi166 – 1705
Beta strandi173 – 1797
Helixi181 – 1866
Beta strandi190 – 1923
Beta strandi217 – 2215
Turni223 – 2253
Beta strandi227 – 2359
Beta strandi237 – 2393
Beta strandi242 – 2476
Beta strandi254 – 2574

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NS2X-ray2.20A/B26-262[»]
4H75X-ray2.10A27-262[»]
4MZFX-ray2.10B50-262[»]
4MZGX-ray1.70B/D50-262[»]
4MZHX-ray2.20A50-262[»]
ProteinModelPortaliQ9Y657.
SMRiQ9Y657. Positions 50-260.

Miscellaneous databases

EvolutionaryTraceiQ9Y657.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 11664Tudor-like domain 1
Add
BLAST
Regioni93 – 986Histone H3K4me3 and H3R8me2a binding
Regioni132 – 19362Tudor-like domain 2
Add
BLAST
Regioni142 – 1421Histone H3K4me3 and H3R8me2a binding
Regioni213 – 26250Tudor-like domain 3
Add
BLAST
Regioni250 – 2523Histone H3K4me3 and H3R8me2a binding

Domaini

The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones (1 Publication, 1 Publication). H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively (1 Publication).1 Publication

Sequence similaritiesi

Belongs to the SPIN/STSY family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG40069.
HOGENOMiHOG000293367.
HOVERGENiHBG000686.
InParanoidiQ9Y657.
OMAiHKDERVQ.
OrthoDBiEOG7CK37K.
PhylomeDBiQ9Y657.
TreeFamiTF332665.

Family and domain databases

InterProiIPR003671. SPIN/Ssty.
IPR029565. Spindlin-1.
[Graphical view]
PANTHERiPTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
PfamiPF02513. Spin-Ssty. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y657-1 [UniParc]FASTAAdd to Basket

« Hide

MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR    50
RNIVGCRIQH GWKEGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL 100
ELNKDERVSA LEVLPDRVAT SRISDAHLAD TMIGKAVEHM FETEDGSKDE 150
WRGMVLARAP VMNTWFYITY EKDPVLYMYQ LLDDYKEGDL RIMPDSNDSP 200
PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP SVYFIKFDDD 250
FHIYVYDLVK TS 262
Length:262
Mass (Da):29,601
Last modified:April 18, 2006 - v3
Checksum:i49F86CBCC7A0AA01
GO

Sequence cautioni

The sequence AAD43035.1 differs from that shown. Reason: Frameshift at position 21.
The sequence AAG38112.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAG48367.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAB66653.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.
The sequence CAG38515.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211A → P.
Corresponds to variant rs34794905 [ dbSNP | Ensembl ].
VAR_053690

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491P → S in BAG52466. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF106682 mRNA. Translation: AAD43035.1. Frameshift.
AF087864 mRNA. Translation: AAG48367.1. Different initiation.
AF317228 mRNA. Translation: AAG38112.1. Different initiation.
AL136719 mRNA. Translation: CAB66653.1. Sequence problems.
BT007314 mRNA. Translation: AAP35978.1.
AK092017 mRNA. Translation: BAG52466.1.
AK289691 mRNA. Translation: BAF82380.1.
AK290009 mRNA. Translation: BAF82698.1.
AK315854 mRNA. Translation: BAF98745.1.
AL353748 Genomic DNA. Translation: CAH72406.1.
CH471089 Genomic DNA. Translation: EAW62753.1.
BC013571 mRNA. No translation available.
BC114515 mRNA. Translation: AAI14516.1.
BC114565 mRNA. Translation: AAI14566.1.
CR533484 mRNA. Translation: CAG38515.1. Sequence problems.
CCDSiCCDS43843.1.
RefSeqiNP_006708.2. NM_006717.2.
UniGeneiHs.146804.

Genome annotation databases

EnsembliENST00000375859; ENSP00000365019; ENSG00000106723.
ENST00000541629; ENSP00000441864; ENSG00000106723.
GeneIDi10927.
KEGGihsa:10927.
UCSCiuc004apy.3. human.

Polymorphism databases

DMDMi93141317.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF106682 mRNA. Translation: AAD43035.1 . Frameshift.
AF087864 mRNA. Translation: AAG48367.1 . Different initiation.
AF317228 mRNA. Translation: AAG38112.1 . Different initiation.
AL136719 mRNA. Translation: CAB66653.1 . Sequence problems.
BT007314 mRNA. Translation: AAP35978.1 .
AK092017 mRNA. Translation: BAG52466.1 .
AK289691 mRNA. Translation: BAF82380.1 .
AK290009 mRNA. Translation: BAF82698.1 .
AK315854 mRNA. Translation: BAF98745.1 .
AL353748 Genomic DNA. Translation: CAH72406.1 .
CH471089 Genomic DNA. Translation: EAW62753.1 .
BC013571 mRNA. No translation available.
BC114515 mRNA. Translation: AAI14516.1 .
BC114565 mRNA. Translation: AAI14566.1 .
CR533484 mRNA. Translation: CAG38515.1 . Sequence problems.
CCDSi CCDS43843.1.
RefSeqi NP_006708.2. NM_006717.2.
UniGenei Hs.146804.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NS2 X-ray 2.20 A/B 26-262 [» ]
4H75 X-ray 2.10 A 27-262 [» ]
4MZF X-ray 2.10 B 50-262 [» ]
4MZG X-ray 1.70 B/D 50-262 [» ]
4MZH X-ray 2.20 A 50-262 [» ]
ProteinModelPortali Q9Y657.
SMRi Q9Y657. Positions 50-260.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116130. 15 interactions.
DIPi DIP-40062N.
IntActi Q9Y657. 6 interactions.
MINTi MINT-1428826.
STRINGi 9606.ENSP00000365019.

PTM databases

PhosphoSitei Q9Y657.

Polymorphism databases

DMDMi 93141317.

Proteomic databases

MaxQBi Q9Y657.
PaxDbi Q9Y657.
PRIDEi Q9Y657.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375859 ; ENSP00000365019 ; ENSG00000106723 .
ENST00000541629 ; ENSP00000441864 ; ENSG00000106723 .
GeneIDi 10927.
KEGGi hsa:10927.
UCSCi uc004apy.3. human.

Organism-specific databases

CTDi 10927.
GeneCardsi GC09P091003.
HGNCi HGNC:11243. SPIN1.
HPAi HPA000162.
MIMi 609936. gene.
neXtProti NX_Q9Y657.
PharmGKBi PA162404504.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG40069.
HOGENOMi HOG000293367.
HOVERGENi HBG000686.
InParanoidi Q9Y657.
OMAi HKDERVQ.
OrthoDBi EOG7CK37K.
PhylomeDBi Q9Y657.
TreeFami TF332665.

Miscellaneous databases

ChiTaRSi SPIN1. human.
EvolutionaryTracei Q9Y657.
GeneWikii SPIN1.
GenomeRNAii 10927.
NextBioi 41511.
PROi Q9Y657.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y657.
CleanExi HS_SPIN1.
Genevestigatori Q9Y657.

Family and domain databases

InterProi IPR003671. SPIN/Ssty.
IPR029565. Spindlin-1.
[Graphical view ]
PANTHERi PTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
Pfami PF02513. Spin-Ssty. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  2. "Cloning, characterization and mapping of human SPIN to human chromosome 9q22.1-22.3."
    Zhang H.L., Yu L., Wang X., Chen Z., Tu Q., Chen J.Q., Ding J.B., Gao J., Zhao S.Y.
    Chin. Sci. Bull. 45:909-914(2000)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Spindlin1, a novel nuclear protein with a role in the transformation of NIH3T3 cells."
    Gao Y., Yue W., Zhang P., Li L., Xie X., Yuan H., Chen L., Liu D., Yan F., Pei X.
    Biochem. Biophys. Res. Commun. 335:343-350(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Tissue: Ovarian carcinoma.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal kidney.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Amygdala, Hippocampus and Trachea.
  7. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  10. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-225.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes."
    Wang W., Chen Z., Mao Z., Zhang H., Ding X., Chen S., Zhang X., Xu R., Zhu B.
    EMBO Rep. 12:1160-1166(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-141 AND TYR-170.
  15. "SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling."
    Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C., Zhou J.N., Jia Y.L., Yue W., Pei X.T.
    Mol. Cancer Res. 10:326-335(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCF7L2, PHOSPHORYLATION AT SER-109 AND SER-124, MUTAGENESIS OF SER-109 AND SER-124, TISSUE SPECIFICITY.
  16. "Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation."
    Zhao Q., Qin L., Jiang F., Wu B., Yue W., Xu F., Rong Z., Yuan H., Xie X., Gao Y., Bai C., Bartlam M., Pei X., Rao Z.
    J. Biol. Chem. 282:647-656(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-262 IN COMPLEX WITH PHOSPHATE IONS, DNA-BINDING, SUBUNIT, DOMAINS TUDOR-LIKE.
  17. "Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1."
    Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.
    Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-262 IN COMPLEX WITH METHYLATED HISTONE H3, MUTAGENESIS OF ASP-184 AND ASP-189.
  18. "Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1."
    Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.
    Genes Dev. 28:622-636(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 50-262 IN COMPLEX WITH METHYLATED HISTONE H3, FUNCTION, INTERACTION WITH TCF7L2, MUTAGENESIS OF TRP-72; TYR-98; PHE-141; GLU-142; TYR-170; TYR-177; ASP-184 AND PHE-251.

Entry informationi

Entry nameiSPIN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y657
Secondary accession number(s): A8K0X6
, B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: April 18, 2006
Last modified: September 3, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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